This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. In about half of the known virus families, the coat that protects the viral genome (DNA or RNA) is a 'spherical'or icosahedral capsid [1, 2]. These capsids are composed of 60*T proteins that are arranged as twelve pentamers and 10(T-1) hexamers at well-defined locations, where T is the triangulation number denoting the number of protein subunits constituting an icosahedral asymmetric unit (T=1, 3, 4, 7, etc.). Capsid proteins must assemble correctly, rapidly, and spontaneously to encapsulate the genomic content so as to propagate an infection in vivo [3]. Elucidating the means by which capsid proteins and the viral genome are self-assembled into full viruses has the potential to assist the development of novel approaches to interfere with the assembly process and ultimately with viral infections. This might shift the paradigm in developing commercial antiviral therapeutics from targeting already-assembled viruses to interrupting assembly of viruses. Simulations of virus assembly inhibition could provide novel confirmation that targeting the assembly process is a viable antiviral strategy.